6BGK
Caspase-3 Mutant- D9A,D28A,T152D
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
| C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | LYS53 |
| A | GLY66 |
| A | THR67 |
| A | ASP68 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| C | ASP192 |
| C | HOH446 |
| A | ASP152 |
| A | GLY153 |
| A | LYS156 |
| C | ILE187 |
| C | ALA191 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue AZI C 301 |
| Chain | Residue |
| B | ASN35 |
| B | HOH434 |
| C | ARG238 |
| C | ARG241 |
| D | THR270 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 201 |
| Chain | Residue |
| B | LYS53 |
| B | GLY66 |
| B | THR67 |
| B | ASP68 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue NA B 202 |
| Chain | Residue |
| B | PHE143 |
| B | ARG144 |
| B | GLY145 |
| B | CYS148 |
| B | LEU151 |
| B | ASP152 |
| B | LYS156 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 203 |
| Chain | Residue |
| B | ARG64 |
| B | THR67 |
| B | ASP70 |
| B | LEU119 |
| B | GLN161 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 204 |
| Chain | Residue |
| B | GLN161 |
| D | SER205 |
| D | TRP206 |
| D | TRP214 |
| D | PHE215 |
| D | GLN261 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CL D 301 |
| Chain | Residue |
| B | GLY153 |
| B | LYS156 |
| D | ILE187 |
| D | ALA191 |
| D | ASP192 |
| D | HOH446 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue AZI D 302 |
| Chain | Residue |
| A | ASN35 |
| C | THR270 |
| D | ARG238 |
| D | ARG241 |
| D | HOH418 |
| site_id | AD1 |
| Number of Residues | 26 |
| Details | binding site for Ac-Asp-Glu-Val-Asp-CMK chain F |
| Chain | Residue |
| A | ARG64 |
| A | HIS121 |
| A | GLY122 |
| A | GLN161 |
| A | CYS163 |
| A | HOH402 |
| B | SER58 |
| B | HOH453 |
| C | TYR204 |
| C | SER205 |
| C | TRP206 |
| C | ARG207 |
| C | ASN208 |
| C | SER209 |
| C | TRP214 |
| C | SER249 |
| C | PHE250 |
| C | HOH416 |
| C | HOH418 |
| C | HOH434 |
| F | HOH101 |
| F | HOH102 |
| F | HOH103 |
| F | HOH104 |
| F | HOH105 |
| F | HOH106 |
| site_id | AD2 |
| Number of Residues | 26 |
| Details | binding site for Ac-Asp-Glu-Val-Asp-CMK chain H |
| Chain | Residue |
| H | HOH105 |
| H | HOH106 |
| A | SER58 |
| A | HOH454 |
| B | ARG64 |
| B | HIS121 |
| B | GLY122 |
| B | GLN161 |
| B | CYS163 |
| B | HOH414 |
| D | TYR204 |
| D | SER205 |
| D | TRP206 |
| D | ARG207 |
| D | ASN208 |
| D | SER209 |
| D | TRP214 |
| D | SER249 |
| D | PHE250 |
| D | HOH420 |
| D | HOH434 |
| D | HOH435 |
| H | HOH101 |
| H | HOH102 |
| H | HOH103 |
| H | HOH104 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P29466","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine; in inhibited form","evidences":[{"source":"PubMed","id":"10213689","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36423631","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 815 |
| Chain | Residue | Details |
| A | THR62 | electrostatic stabiliser |
| A | SER63 | electrostatic stabiliser |
| A | HIS121 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLY122 | electrostatic stabiliser |
| A | CYS163 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 815 |
| Chain | Residue | Details |
| C | THR237 | electrostatic stabiliser |
| C | ARG238 | electrostatic stabiliser |
